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Preparation of Recombinant RNase Single-Chain Antibody Fusion Proteins

Molecular Biotechnology, 2002
This article describes the construction, expression, and purification of RNase single-chain antibody fusion proteins. To construct a fusion protein, the gene for each moiety, the RNase and the binding ligand, is modified separately to contain complementary DNA encoding a 13 amino acid spacer that separates the RNase from the binding moiety. Appropriate
D L, Newton, S M, Rybak
openaire   +3 more sources

Population pharmacokinetics of recombinant factor VIII Fc fusion protein

Clinical Pharmacology in Drug Development, 2014
AbstractPopulation pharmacokinetics (PK) of FVIII activity‐time profiles following recombinant factor VIII Fc fusion protein (rFVIIIFc) and recombinant factor VIII (rFVIII) dosing were evaluated in previously treated patients with severe hemophilia A (from two clinical trials).
Ivan, Nestorov   +5 more
openaire   +2 more sources

Recombinant Human Hb‐SOD Fusion Proteins

2013
Hemoglobin (Hb) can produce reactive oxygen species, including superoxide anions, which are intrinsically toxic. Superoxide dismutase (SOD) is present in red blood cells (RBCs) and provides important protection against such oxidative stress. Upon hemolysis, Hb becomes released from the RBCs and the normal protection systems involving SOD and catalase ...
Marie Grey   +2 more
openaire   +1 more source

Recombinant Baculovirus Vectors Expressing Glutathione–S–Transferase Fusion Proteins

Nature Biotechnology, 1993
Recombinant baculoviruses are a popular means of producing heterologous protein in eukaryotic cells. Purification of recombinant proteins away from the insect cell background can, however, remain an obstacle for many developments. Recently, prokaryotic fusion protein expression systems have been developed allowing single-step purification of the ...
A H, Davies, J B, Jowett, I M, Jones
openaire   +2 more sources

Architecting Multicompartmentalized, Giant Vesicles with Recombinant Fusion Proteins

Biomacromolecules
We present a straightforward strategy for constructing giant, multicompartmentalized vesicles using recombinant fusion proteins. Our method leverages the self-assembly of globule-zipper-elastin-like polypeptide fusion protein complexes in aqueous conditions, eliminating the need for organic solvents and chemical conjugation.
Jooyong Shin   +3 more
openaire   +2 more sources

Self-cleaving fusion tags for recombinant protein production

Biotechnology Letters, 2011
Fusion expression is a common practice for recombinant protein production. Some fusion tags confer solubility on the target protein whereas others provide affinity handles that facilitate purification. However, the tag usually needs to be removed from the final product, which involves using expensive proteases or hazardous chemicals and requires ...
openaire   +2 more sources

Antigenicity of a recombinant Ro (SS‐A) fusion protein

Arthritis & Rheumatism, 1990
AbstractThe antigenicity of the 60‐kd human Ro (SS‐A) synthesized in vitro from its complementary DNA as a β‐galactosidase fusion protein (β‐gal—Ro) was evaluated by Western blotting. In this analysis, almost all the anti‐Ro (SS‐A)‐positive sera that bound β‐gal‐Ro also bound affinity‐purified 60‐kd human Ro (SS‐A) (P > 0.005).
J A, James   +6 more
openaire   +2 more sources

Recombinant fusion protein of albumin-retinol binding protein inactivates stellate cells

Biochemical and Biophysical Research Communications, 2012
Quiescent pancreatic- (PSCs) and hepatic- (HSCs) stellate cells store vitamin A (retinol) in lipid droplets via retinol binding protein (RBP) receptor and, when activated by profibrogenic stimuli, they transform into myofibroblast-like cells which play a key role in the fibrogenesis.
Soyoung, Choi   +6 more
openaire   +2 more sources

Recombinant peptide fusion proteins enable palladium nanoparticle growth

Materials Letters, 2019
Abstract The soluble fraction of bacterial lysates containing repeat units of a metal binding domain (Pd4) fused to the carrier protein Green Fluorescent Protein (GFPuv) was used to direct palladium nanoparticle synthesis on the order of 2 nm. Characterization confirmed the synthesis of highly ordered materials, as evident by microscopy and elemental
Mosleh, Imann   +4 more
openaire   +2 more sources

Different Approaches to Stabilize a Recombinant Fusion Protein

Nature Biotechnology, 1989
We have used a fusion protein between staphylococcal protein A and E. coli β–galactosidase as a model system to investigate different approaches to stabilize recombinant gene products. First, growth conditions were adapted to preferentially produce insoluble inclusion bodies.
Halldis Hellebust   +4 more
openaire   +1 more source

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